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Artikel ; Online: Xenopus

Liu, Junjun / Zhang, Chuanmao

Biophysics reports

2022 Band 9, Heft 4, Seite(n) 195–205

Abstract: ... ...

Abstract	Xenopus
Sprache	Englisch
Erscheinungsdatum	2022-07-18
Erscheinungsland	China
Dokumenttyp	Journal Article
ISSN	2364-3420
ISSN (online)	2364-3420
DOI	10.52601/bpr.2023.230016
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Live-cell fluorescence imaging of ciliary dynamics.

Lü, Quanlong / Zhang, Chuanmao / Westlake, Christopher J

Biophysics reports

2023 Band 7, Heft 2, Seite(n) 101–110

Abstract: The cilium was one of the first organelles observed through a microscope. Motile cilia appear as oscillating cell appendages and have long been recognized to function in cell motility. In contrast, the far more widespread non-motile cilia, termed primary ...

Abstract	The cilium was one of the first organelles observed through a microscope. Motile cilia appear as oscillating cell appendages and have long been recognized to function in cell motility. In contrast, the far more widespread non-motile cilia, termed primary cilia, were thought to be vestigial and largely ignored following their initial description over a century ago. Only in the last two decades has the critical function of primary cilia been elucidated. Primary cilia play essential roles in signal transduction, chemical sensation, mechanosensation and light detection. Various microscopy approaches have been important for characterizing the structure, dynamics and function of the cilia. In this review, we discuss the application of live-cell imaging technologies and their contribution to our current understanding of ciliary processes.
Sprache	Englisch
Erscheinungsdatum	2023-05-23
Erscheinungsland	China
Dokumenttyp	Journal Article
ISSN	2364-3420
ISSN (online)	2364-3420
DOI	10.52601/bpr.2021.210005
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: TIP60 acetylation of Bub1 regulates centromeric H2AT120 phosphorylation for faithful chromosome segregation.

Sun, Mengjie / Yang, Biying / Xin, Guangwei / Wang, Yao / Luo, Jia / Jiang, Qing / Zhang, Chuanmao

Science China. Life sciences

2024

Abstract: Proper function of the centromeres ensures correct attachment of kinetochores to spindle microtubules and faithful chromosome segregation in mitosis. Defects in the integrity and function of centromeres can result in chromosome missegregation and genomic ...

Abstract	Proper function of the centromeres ensures correct attachment of kinetochores to spindle microtubules and faithful chromosome segregation in mitosis. Defects in the integrity and function of centromeres can result in chromosome missegregation and genomic instability. Bub1 is essential for the mitotic centromere dynamics, yet the underlying molecular mechanisms remain largely unclear. Here, we demonstrate that TIP60 acetylates Bub1 at K424 and K431 on kinetochores in early mitosis. This acetylation increases the kinase activity of Bub1 to phosphorylate centromeric histone H2A at T120 (H2ApT120), which recruits Aurora B and Shugoshin 1 (Sgo1) to regulate centromere integrity, protect centromeric cohesion, and ensure the subsequent faithful chromosome segregation. Expression of the non-acetylated Bub1 mutant reduces its kinase activity, decreases the level of H2ApT120, and disrupts the recruitment of centromere proteins and chromosome congression, leading to genomic instability of daughter cells. When cells exit mitosis, HDAC1-regulated deacetylation of Bub1 decreases H2ApT120 levels and thereby promotes the departure of centromeric CPC and Sgo1, ensuring timely centromeres disassembly. Collectively, our results reveal a molecular mechanism by which the acetylation and deacetylation cycle of Bub1 modulates the phosphorylation of H2A at T120 for recruitment of Aurora B and Sgo1 to the centromeres, ensuring faithful chromosome segregation during mitosis.
Sprache	Englisch
Erscheinungsdatum	2024-05-17
Erscheinungsland	China
Dokumenttyp	Journal Article
ZDB-ID	2546732-3
ISSN	1869-1889 ; 1674-7305
ISSN (online)	1869-1889
ISSN	1674-7305
DOI	10.1007/s11427-023-2604-8
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: NuSAP regulates microtubule flux and Kif2A localization to ensure accurate chromosome congression.

Sun, Mengjie / Wang, Yao / Xin, Guangwei / Yang, Biying / Jiang, Qing / Zhang, Chuanmao

The Journal of cell biology

2023 Band 223, Heft 2

Abstract: Precise chromosome congression and segregation requires the proper assembly of a steady-state metaphase spindle, which is dynamic and maintained by continuous microtubule flux. NuSAP is a microtubule-stabilizing and -bundling protein that promotes ... ...

Abstract	Precise chromosome congression and segregation requires the proper assembly of a steady-state metaphase spindle, which is dynamic and maintained by continuous microtubule flux. NuSAP is a microtubule-stabilizing and -bundling protein that promotes chromosome-dependent spindle assembly. However, its function in spindle dynamics remains unclear. Here, we demonstrate that NuSAP regulates the metaphase spindle length control. Mechanistically, NuSAP facilitates kinetochore capture and spindle assembly by promoting Eg5 binding to microtubules. It also prevents excessive microtubule depolymerization through interaction with Kif2A, which reduces Kif2A spindle-pole localization. NuSAP is phosphorylated by Aurora A at Ser-240 during mitosis, and this phosphorylation promotes its interaction with Kif2A on the spindle body and reduces its localization with the spindle poles, thus maintaining proper spindle microtubule flux. NuSAP knockout resulted in the formation of shorter spindles with faster microtubule flux and chromosome misalignment. Taken together, we uncover that NuSAP participates in spindle assembly, dynamics, and metaphase spindle length control through the regulation of microtubule flux and Kif2A localization.
Mesh-Begriff(e)	Humans ; Chromosome Segregation ; HeLa Cells ; Kinesins/genetics ; Kinesins/metabolism ; Kinetochores/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/genetics ; Microtubules/metabolism ; Mitosis ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism
Chemische Substanzen	Kinesins (EC 3.6.4.4) ; Microtubule-Associated Proteins ; KIF2A protein, human ; NUSAP1 protein, human
Sprache	Englisch
Erscheinungsdatum	2023-12-20
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202108070
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.

Tai, Linhua / Zhu, Yun / Ren, He / Huang, Xiaojun / Zhang, Chuanmao / Sun, Fei

Protein & cell

2022 Band 13, Heft 10, Seite(n) 760–777

Abstract: The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 Å resolution cryo-electron microscopic (cryo-EM) structure of the outer rings ...

Abstract	The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 Å resolution cryo-electron microscopic (cryo-EM) structure of the outer rings containing nuclear ring (NR) and cytoplasmic ring (CR) from the Xenopus laevis NPC, with local resolutions reaching 4.9 Å. With the aid of AlphaFold2, we managed to build a pseudoatomic model of the outer rings, including the Y complexes and flanking components. In this most comprehensive and accurate model of outer rings to date, the almost complete Y complex structure exhibits much tighter interaction in the hub region. In addition to two copies of Y complexes, each asymmetric subunit in CR contains five copies of Nup358, two copies of the Nup214 complex, two copies of Nup205 and one copy of newly identified Nup93, while that in NR contains one copy of Nup205, one copy of ELYS and one copy of Nup93. These in-depth structural features represent a great advance in understanding the assembly of NPCs.
Mesh-Begriff(e)	Animals ; Artificial Intelligence ; Cryoelectron Microscopy ; Nuclear Pore/chemistry ; Nuclear Pore/metabolism ; Nuclear Pore/ultrastructure ; Oocytes/metabolism ; Xenopus laevis
Sprache	Englisch
Erscheinungsdatum	2022-01-11
Erscheinungsland	Germany
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2543451-2
ISSN	1674-8018 ; 1674-800X
ISSN (online)	1674-8018
ISSN	1674-800X
DOI	10.1007/s13238-021-00895-y
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Cartwheel disassembly regulated by CDK1-Cyclin B kinase allows human centriole disengagement and licensing.

Huang, Fan / Xu, Xiaowei / Xin, Guangwei / Zhang, Boyan / Jiang, Qing / Zhang, Chuanmao

The Journal of biological chemistry

2022 , Seite(n) 102658

Abstract: Cartwheel assembly is considered the first step in the initiation of procentriole biogenesis; however, the reason for persistence of the assembled human cartwheel structure from S phase to late mitosis remains unclear. Here, we demonstrate mainly using ... ...

Abstract	Cartwheel assembly is considered the first step in the initiation of procentriole biogenesis; however, the reason for persistence of the assembled human cartwheel structure from S phase to late mitosis remains unclear. Here, we demonstrate mainly using cell synchronization, RNA interference, immunofluorescence and time-lapse-microscopy, biochemical analysis and methods that the cartwheel persistently assembles and maintains centriole engagement and centrosome integrity during S phase to late G2 phase. Blockade of the continuous accumulation of centriolar Sas-6, a major cartwheel protein, after procentriole formation induces premature centriole disengagement and disrupts pericentriolar matrix integrity. Additionally, we determined that during mitosis, CDK1-Cyclin B phosphorylates Sas-6 at T495 and S510, disrupting its binding to cartwheel component STIL and pericentriolar component Nedd1 and promoting cartwheel disassembly and centriole disengagement. Perturbation of this phosphorylation maintains the accumulation of centriolar Sas-6 and retains centriole engagement during mitotic exit, which results in the inhibition of centriole reduplication. Collectively, these data demonstrate that persistent cartwheel assembly after procentriole formation maintains centriole engagement and that this configuration is relieved through phosphorylation of Sas-6 by CDK1-Cyclin B during mitosis in human cells.
Sprache	Englisch
Erscheinungsdatum	2022-11-07
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102658
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: The equilibrium of ubiquitination and deubiquitination at PLK1 regulates sister chromatid separation.

Liu, Junjun / Zhang, Chuanmao

Cellular and molecular life sciences : CMLS

2017 Band 74, Heft 12, Seite(n) 2127–2134

Abstract: PLK1 regulates almost every aspect of mitotic events, including mitotic entry, spindle assembly, chromosome alignment, sister chromatid segregation, metaphase-anaphase transition, cytokinesis, etc. In regulating the chromosome alignment and sister ... ...

Abstract	PLK1 regulates almost every aspect of mitotic events, including mitotic entry, spindle assembly, chromosome alignment, sister chromatid segregation, metaphase-anaphase transition, cytokinesis, etc. In regulating the chromosome alignment and sister chromatid segregation, PLK1 has to be localized to and removed from kinetochores at the right times, and the underlying mechanism that regulates PLK1 both spatially and temporally only became clearer recently. It has been found that deubiquitination and ubiquitination of PLK1 are responsible for its localization to and dissociation from the kinetochores, respectively. The equilibrium of this ubiquitination and deubiquitination plays an important role in regulating proper chromosome alignment and timely sister chromatid segregation. Here, we summarize and discuss the recent findings in investigating the spatial and temporal regulation of PLK1 during chromosome alignment and sister chromatid segregation.
Mesh-Begriff(e)	Animals ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Chromatids/metabolism ; Humans ; Kinetochores/metabolism ; Protein Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Substrate Specificity ; Ubiquitination ; Polo-Like Kinase 1
Chemische Substanzen	Cell Cycle Proteins ; Proto-Oncogene Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Sprache	Englisch
Erscheinungsdatum	2017-02-10
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-017-2457-5
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: PLK4-phosphorylated NEDD1 facilitates cartwheel assembly and centriole biogenesis initiations.

Chi, Wangfei / Wang, Gang / Xin, Guangwei / Jiang, Qing / Zhang, Chuanmao

The Journal of cell biology

2020 Band 220, Heft 1

Abstract: Centrosome duplication occurs under strict spatiotemporal regulation once per cell cycle, and it begins with cartwheel assembly and daughter centriole biogenesis at the lateral sites of the mother centrioles. However, although much of this process is ... ...

Abstract	Centrosome duplication occurs under strict spatiotemporal regulation once per cell cycle, and it begins with cartwheel assembly and daughter centriole biogenesis at the lateral sites of the mother centrioles. However, although much of this process is understood, how centrosome duplication is initiated remains unclear. Here, we show that cartwheel assembly followed by daughter centriole biogenesis is initiated on the NEDD1-containing layer of the pericentriolar material (PCM) by the recruitment of SAS-6 to the mother centriole under the regulation of PLK4. We found that PLK4-mediated phosphorylation of NEDD1 at its S325 amino acid residue directly promotes both NEDD1 binding to SAS-6 and recruiting SAS-6 to the centrosome. Overexpression of phosphomimicking NEDD1 mutant S325E promoted cartwheel assembly and daughter centriole biogenesis initiations, whereas overexpression of nonphosphorylatable NEDD1 mutant S325A abolished the initiations. Collectively, our results demonstrate that PLK4-regulated NEDD1 facilitates initiation of the cartwheel assembly and of daughter centriole biogenesis in mammals.
Mesh-Begriff(e)	Amino Acid Sequence ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Centrioles/metabolism ; Centrosome/metabolism ; HEK293 Cells ; Humans ; Microtubule-Associated Proteins/metabolism ; Models, Biological ; Mutant Proteins/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Binding ; Protein-Serine-Threonine Kinases/metabolism ; Tubulin/metabolism
Chemische Substanzen	Cell Cycle Proteins ; Microtubule-Associated Proteins ; Mutant Proteins ; NEDD1 protein, human ; SASS6 protein, human ; Tubulin ; Phosphoserine (17885-08-4) ; PLK4 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Sprache	Englisch
Erscheinungsdatum	2020-12-21
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202002151
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Stay in touch with the endoplasmic reticulum.

Sun, Sha / Zhao, Gan / Jia, Mingkang / Jiang, Qing / Li, Shulin / Wang, Haibin / Li, Wenjing / Wang, Yunyun / Bian, Xin / Zhao, Yan G / Huang, Xun / Yang, Ge / Cai, Huaqing / Pastor-Pareja, Jose C / Ge, Liang / Zhang, Chuanmao / Hu, Junjie

Science China. Life sciences

2024 Band 67, Heft 2, Seite(n) 230–257

Abstract: The endoplasmic reticulum (ER), which is composed of a continuous network of tubules and sheets, forms the most widely distributed membrane system in eukaryotic cells. As a result, it engages a variety of organelles by establishing membrane contact sites ...

Abstract	The endoplasmic reticulum (ER), which is composed of a continuous network of tubules and sheets, forms the most widely distributed membrane system in eukaryotic cells. As a result, it engages a variety of organelles by establishing membrane contact sites (MCSs). These contacts regulate organelle positioning and remodeling, including fusion and fission, facilitate precise lipid exchange, and couple vital signaling events. Here, we systematically review recent advances and converging themes on ER-involved organellar contact. The molecular basis, cellular influence, and potential physiological functions for ER/nuclear envelope contacts with mitochondria, Golgi, endosomes, lysosomes, lipid droplets, autophagosomes, and plasma membrane are summarized.
Mesh-Begriff(e)	Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Cell Membrane/metabolism ; Mitochondria/metabolism ; Lysosomes/metabolism ; Endosomes/metabolism
Sprache	Englisch
Erscheinungsdatum	2024-01-04
Erscheinungsland	China
Dokumenttyp	Systematic Review ; Journal Article ; Review
ZDB-ID	2546732-3
ISSN	1869-1889 ; 1674-7305
ISSN (online)	1869-1889
ISSN	1674-7305
DOI	10.1007/s11427-023-2443-9
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Aurora B regulates PP1γ-Repo-Man interactions to maintain the chromosome condensation state.

Xin, Guangwei / Fu, Jingyan / Luo, Jia / Deng, Zhaoxuan / Jiang, Qing / Zhang, Chuanmao

The Journal of biological chemistry

2020 Band 295, Heft 43, Seite(n) 14780–14788

Abstract: The mitotic kinase Aurora B regulates the condensation of chromatin into chromosomes by phosphorylating chromatin proteins during early mitosis, whereas the phosphatase PP1γ performs the opposite function. The roles of Aurora B and PP1γ must be tightly ... ...

Abstract	The mitotic kinase Aurora B regulates the condensation of chromatin into chromosomes by phosphorylating chromatin proteins during early mitosis, whereas the phosphatase PP1γ performs the opposite function. The roles of Aurora B and PP1γ must be tightly coordinated to maintain chromosomes at a high phosphorylation state, but the precise mechanisms regulating their function remain largely unclear. Here, mainly through immunofluorescence microscopy and co-immunoprecipitation assays, we find that dissociation of PP1γ from chromosomes is essential for maintaining chromosome phosphorylation. We uncover that PP1γ is recruited to mitotic chromosomes by its regulatory subunit Repo-Man in the absence of Aurora B activity and that Aurora B regulates dissociation of PP1γ by phosphorylating and disrupting PP1γ-Repo-Man interactions on chromatin. Overexpression of Repo-Man mutants that cannot be phosphorylated or inhibition of Aurora B kinase activity resulted in the retention of PP1γ on chromatin and prolonged the chromatin condensation process; a similar outcome was caused by the ectopic targeting of PP1γ to chromatin. Together, our findings reveal a novel regulation mechanism of chromatin condensation in which Aurora B counteracts PP1γ activity by releasing PP1γ from Repo-Man and may have important implications for understanding the regulations of dynamic structural changes of the chromosomes in mitosis.
Mesh-Begriff(e)	Aurora Kinase B/metabolism ; Carrier Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Chromatin/metabolism ; Chromosomes, Human/metabolism ; HeLa Cells ; Humans ; Mitosis ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Interaction Maps ; Protein Phosphatase 1/metabolism
Chemische Substanzen	CDCA2 protein, human ; Carrier Proteins ; Cell Cycle Proteins ; Chromatin ; Nuclear Proteins ; Aurora Kinase B (EC 2.7.11.1) ; Protein Phosphatase 1 (EC 3.1.3.16)
Sprache	Englisch
Erscheinungsdatum	2020-09-16
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.AC120.012772
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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